Fig. 30.3 The four shorter helices (bright red) of the tetrameric potassium channel orient their negatively polarized C ...
Fig. 30.4 Crystal structure of the bacterial potassium channel KcsA in the open state. The channel forms a tetramer (a),...
Fig. 30.5 Comparison of the tetrameric ion filter of the highly selective potassium channel KcsA from Streptomyces livid...
Fig. 30.9 (a) Cryo-EM structure of the human NaV-1.7 channel. The central part of the channel is embedded in the membran...
Fig. 30.12 Cryo-EM structure of the human NaV-1.7 channel with the highly toxic tetradoxin 30.20 from the fugu fish. The...
Fig. 30.13 (a) (a) Cryo-EM structure of the rabbit CaV channel with the bound calcium antagonist nifedipine 30.24. The d...
Fig. 30.14 Superposition of the binding modes of verapamil 30.26, diltiazem 30.25 and nifedipine 30.24 in the rabbit CaV...
Fig. 30.15 In the cryo-EM structure, the nicotinic acetylcholine receptor has a diameter of 80 Å and is 125 Å long (a)...
Fig. 30.17 Binding of an agonist (here epibatidine, 30.29) or antagonist (here α-conotoxin 30.31) to the ligand-binding...
Fig. 30.18 Crystal structure of the ligand-binding domain of the nicotinic acetylcholine receptor with the bound agonist...
Fig. 30.20 Cryo-EM structure of the GABA-A receptor showing two bound GABA molecules (purple surface) and the channel bl...
Fig. 30.21 Comparison of the cryo-EM structures of the GABA-A receptor with bound GABA (and picrotoxinin, cf. Fig. 30.20...
Fig. 30.23 Cryo-EM structures of the GABA-A receptor with bound GABA 30.35 and diazepam 30.40 (left), phenobarbital 30.3...
Fig. 30.24 (a) Systematic bioisosteric replacement with exchange of substituents R1-R4 yields numerous benzodiazepines w...
Fig. 30.25 Two long helices orient their positively polarized, N-terminal ends toward the narrowest position in the chan...
Fig. 30.27 Cryo-EM structure of the H+/K+-ATPase with the inhibitor tegoprazan 30.47. The drug binds near the opening of...
Fig. 30.28 Crystal or cryo-EM structures of different situations along the transport cycle of ABC transporters. They are...
Fig. 30.29 Crystal structure of the porin from the bacteria Rhodobacter capsulatus. Each pore of the trimeric proteins (...
Fig. 30.30 Gramicidin A, (Val–Gly–Ala–Leu–Ala–Val3–(Trp–Leu)3–Trp–ethanolamine) is made up of 15 alter...
Fig. 30.31 Nonactin represents a chelating Ligand to coordinate potassium ions. It wraps optimally around the ion and ca...
Fig. 30.32 a) Crystal structure of bovine aquaporin-1. Only one pore of the fourfold protein is shown. It widens in a fu...